tetano
Editor, Senior Moderator
Virol J
. 2024 Aug 12;21(1):186.
doi: 10.1186/s12985-024-02460-5. SARS-CoV-2 nucleocapsid protein promotes self-deacetylation by inducing HDAC6 to facilitate viral replication
Arpita Mukherjee[SUP] 1 [/SUP], Mahadeb Lo[SUP] 1 [/SUP], Pritam Chandra[SUP] 1 [/SUP], Ratul Datta Chaudhuri[SUP] 1 [/SUP], Papiya De[SUP] 1 [/SUP], Shanta Dutta[SUP] 1 [/SUP], Mamta Chawla-Sarkar[SUP] 2 [/SUP]
Affiliations
Background: The global outbreak of COVID-19 caused by the SARS-CoV-2 has led to millions of deaths. This unanticipated emergency has prompted virologists across the globe to delve deeper into the intricate dynamicity of the host-virus interface with an aim to identify antiviral targets and elucidate host and viral determinants of severe disease.
Aim: The present study was undertaken to analyse the role of histone deacetylase 6 (HDAC6) in regulating SARS-CoV-2 infection.
Results: Gradual increase in HDAC6 expression was observed in different SARS-CoV-2-permissive cell lines following SARS-CoV-2 infection. The SARS-CoV-2 nucleocapsid protein (N protein) was identified as the primary viral factor responsible for upregulating HDAC6 expression. Downregulation of HDAC6 using shRNA or a specific inhibitor tubacin resulted in reduced viral replication suggesting proviral role of its deacetylase activity. Further investigations uncovered the interaction of HDAC6 with stress granule protein G3BP1 and N protein during infection. HDAC6-mediated deacetylation of SARS-CoV-2 N protein was found to be crucial for its association with G3BP1.
Conclusion: This study provides valuable insights into the molecular mechanisms underlying the disruption of cytoplasmic stress granules during SARS-CoV-2 infection and highlights the significance of HDAC6 in the process.
Keywords: Deacetylation; G3BP1; HDAC6; SARS-CoV-2; Stress granules (SGs).
. 2024 Aug 12;21(1):186.
doi: 10.1186/s12985-024-02460-5. SARS-CoV-2 nucleocapsid protein promotes self-deacetylation by inducing HDAC6 to facilitate viral replication
Arpita Mukherjee[SUP] 1 [/SUP], Mahadeb Lo[SUP] 1 [/SUP], Pritam Chandra[SUP] 1 [/SUP], Ratul Datta Chaudhuri[SUP] 1 [/SUP], Papiya De[SUP] 1 [/SUP], Shanta Dutta[SUP] 1 [/SUP], Mamta Chawla-Sarkar[SUP] 2 [/SUP]
Affiliations
- PMID: 39135075
- PMCID: PMC11321199
- DOI: 10.1186/s12985-024-02460-5
Background: The global outbreak of COVID-19 caused by the SARS-CoV-2 has led to millions of deaths. This unanticipated emergency has prompted virologists across the globe to delve deeper into the intricate dynamicity of the host-virus interface with an aim to identify antiviral targets and elucidate host and viral determinants of severe disease.
Aim: The present study was undertaken to analyse the role of histone deacetylase 6 (HDAC6) in regulating SARS-CoV-2 infection.
Results: Gradual increase in HDAC6 expression was observed in different SARS-CoV-2-permissive cell lines following SARS-CoV-2 infection. The SARS-CoV-2 nucleocapsid protein (N protein) was identified as the primary viral factor responsible for upregulating HDAC6 expression. Downregulation of HDAC6 using shRNA or a specific inhibitor tubacin resulted in reduced viral replication suggesting proviral role of its deacetylase activity. Further investigations uncovered the interaction of HDAC6 with stress granule protein G3BP1 and N protein during infection. HDAC6-mediated deacetylation of SARS-CoV-2 N protein was found to be crucial for its association with G3BP1.
Conclusion: This study provides valuable insights into the molecular mechanisms underlying the disruption of cytoplasmic stress granules during SARS-CoV-2 infection and highlights the significance of HDAC6 in the process.
Keywords: Deacetylation; G3BP1; HDAC6; SARS-CoV-2; Stress granules (SGs).